FliT function was primarily investigated in Salmonella typhimurium [Kutsukake94a, Fraser99, Bennett01, Yamamoto06a]. FliT, along with FliS and FlgN, may function as cytoplasmic, substrate-specific chaperones of the flagellar export system. They share several similarities with other type III cytoplasmic chaperone family members [Kutsukake94a]. Affinity blot analysis showed that FliT binds in vitro to flagellar cap subunits (FliD) [Fraser99], suggesting that FliT may act as a chaperone which aids in the export and prevents premature aggregation of the FliD flagellar cap component [Bennett01]. Gel filtration chromatography indicate that FliT exists as a homodimer in the cytosol and that these homodimers bind to monomers of FliD to form heterotrimeric chaperone-substrate complexes [Bennett01].